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| {{STRUCTURE_1xfb| PDB=1xfb | SCENE= }} | | {{STRUCTURE_1xfb| PDB=1xfb | SCENE= }} |
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| '''Human Brain Fructose 1,6-(bis)phosphate Aldolase (C isozyme)'''
| | ===Human Brain Fructose 1,6-(bis)phosphate Aldolase (C isozyme)=== |
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| ==Overview==
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| Fructose-1,6-(bis)phosphate aldolase is a ubiquitous enzyme that catalyzes the reversible aldol cleavage of fructose-1,6-(bis)phosphate and fructose 1-phosphate to dihydroxyacetone phosphate and either glyceral-dehyde-3-phosphate or glyceraldehyde, respectively. Vertebrate aldolases exist as three isozymes with different tissue distributions and kinetics: aldolase A (muscle and red blood cell), aldolase B (liver, kidney, and small intestine), and aldolase C (brain and neuronal tissue). The structures of human aldolases A and B are known and herein we report the first structure of the human aldolase C, solved by X-ray crystallography at 3.0 A resolution. Structural differences between the isozymes were expected to account for isozyme-specific activity. However, the structures of isozymes A, B, and C are the same in their overall fold and active site structure. The subtle changes observed in active site residues Arg42, Lys146, and Arg303 are insufficient to completely account for the tissue-specific isozymic differences. Consequently, the structural analysis has been extended to the isozyme-specific residues (ISRs), those residues conserved among paralogs. A complete analysis of the ISRs in the context of this structure demonstrates that in several cases an amino acid residue that is conserved among aldolase C orthologs prevents an interaction that occurs in paralogs. In addition, the structure confirms the clustering of ISRs into discrete patches on the surface and reveals the existence in aldolase C of a patch of electronegative residues localized near the C terminus. Together, these structural changes highlight the differences required for the tissue and kinetic specificity among aldolase isozymes.
| | The line below this paragraph, {{ABSTRACT_PUBMED_15537755}}, adds the Publication Abstract to the page |
| | (as it appears on PubMed at http://www.pubmed.gov), where 15537755 is the PubMed ID number. |
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| | {{ABSTRACT_PUBMED_15537755}} |
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| ==About this Structure== | | ==About this Structure== |
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| [[Category: Structural enzymology]] | | [[Category: Structural enzymology]] |
| [[Category: Structure/function]] | | [[Category: Structure/function]] |
| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 14:57:16 2008'' | | |
| | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 00:34:18 2008'' |
